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showing 10 items of 2320 documents

On the arithmetically Cohen-Macaulay property for sets of points in multiprojective spaces

2017

We study the arithmetically Cohen-Macaulay (ACM) property for finite sets of points in multiprojective spaces, especially ( P 1 ) n (\mathbb P^1)^n . A combinatorial characterization, the ( ⋆ ) (\star ) -property, is known in P 1 × P 1 \mathbb P^1 \times \mathbb P^1 . We propose a combinatorial property, ( ⋆ s ) (\star _s) with 2 ≤ s ≤ n 2\leq s\leq n , that directly generalizes the ( ⋆ ) (\star ) -property to ( P 1 ) n (\mathbb P^1)^n for larger n n . We show that X X is ACM if and only if it satisfies the ( ⋆ n ) (\star _n) -property. The main tool for several of our results is an extension to the multiprojective setting of certain liaison methods in projective space.

Property (philosophy)General MathematicsStar (game theory)Arithmetically Cohen-Macaulay; Linkage; Points in multiprojective spacescohen- macaulayCharacterization (mathematics)Commutative Algebra (math.AC)01 natural sciencesCombinatoricsMathematics - Algebraic GeometryPoints in multiprojective spaces0103 physical sciencesFOS: MathematicsProjective space0101 mathematicsFinite setAlgebraic Geometry (math.AG)multiprojective spacesMathematicsDiscrete mathematicsMathematics::Commutative AlgebraLinkageArithmetically Cohen-Macaulay Linkage Points in multiprojective spacesApplied Mathematics010102 general mathematicsExtension (predicate logic)Mathematics - Commutative AlgebraArithmetically Cohen-MacaulaypointsSettore MAT/02 - Algebracohen- macaulay multiprojective spaces points010307 mathematical physicsSettore MAT/03 - Geometria
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The Role of Low Complexity Regions in Protein Interaction Modes: An Illustration in Huntingtin

2021

Low complexity regions (LCRs) are very frequent in protein sequences, generally having a lower propensity to form structured domains and tending to be much less evolutionarily conserved than globular domains. Their higher abundance in eukaryotes and in species with more cellular types agrees with a growing number of reports on their function in protein interactions regulated by post-translational modifications. LCRs facilitate the increase of regulatory and network complexity required with the emergence of organisms with more complex tissue distribution and development. Although the low conservation and structural flexibility of LCRs complicate their study, evolutionary studies of proteins …

Protein Conformation alpha-Helical0301 basic medicineNetwork complexityHuntingtinintrinsically disordered regionsAmino Acid MotifsComputational biologyBiologyprotein interactionsArticlecompositionally biased regionsCatalysisProtein–protein interactionlcsh:ChemistryEvolution MolecularInorganic ChemistryLow complexity03 medical and health sciencesProtein DomainsProtein Interaction MappingAnimalsHumansp300-CBP Transcription FactorsAmino Acid SequenceProtein Interaction MapsHuntingtinTissue distributionPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyHuntingtin Protein030102 biochemistry & molecular biologyOrganic ChemistryNuclear Proteinsp120 GTPase Activating ProteinGeneral MedicineMultiple modesSynapsinslow complexity regionsComputer Science ApplicationshomorepeatsMicroscopy Electron030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Sequence AlignmentFunction (biology)Protein BindingInternational Journal of Molecular Sciences
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Mechanism‐Dependent Modulation of Ultrafast Interfacial Water Dynamics in Intrinsically Disordered Protein Complexes

2018

Abstract The recognition of intrinsically disordered proteins (IDPs) is highly dependent on dynamics owing to the lack of structure. Here we studied the interplay between dynamics and molecular recognition in IDPs with a combination of time‐resolving tools on timescales ranging from femtoseconds to nanoseconds. We interrogated conformational dynamics and surface water dynamics and its attenuation upon partner binding using two IDPs, IBB and Nup153FG, both of central relevance to the nucleocytoplasmic transport machinery. These proteins bind the same nuclear transport receptor (Importinβ) with drastically different binding mechanisms, coupled folding–binding and fuzzy complex formation, resp…

Protein ConformationSolvation Dynamicsprotein–protein interactions010402 general chemistryIntrinsically disordered proteins01 natural sciencestime-resolved spectroscopyCatalysisProtein–protein interactionMolecular recognitionnucleocytoplasmic transport010405 organic chemistryMechanism (biology)ChemistryCommunicationWaterGeneral Chemistrybeta KaryopherinsCommunications0104 chemical sciencesIntrinsically Disordered ProteinsNucleocytoplasmic TransportModulationChemical physicsThermodynamicsTime-resolved spectroscopyNuclear transportAngewandte Chemie International Edition
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New Insights into Protein (Un)Folding Dynamics.

2015

A fundamental open problem in biophysics is how the folded structure of the main chain (MC) of a protein is determined by the physics of the interactions between the side-chains (SCs). All-atom molecular dynamics simulations of a model protein (Trp-cage) revealed that strong correlations between the motions of the SCs and the MC occur transiently at 380 K in unfolded segments of the protein, and during the simulations of the whole amino-acid sequence at 450 K. The high correlation between the SC and MC fluctuations is a fundamental property of the unfolded state and is also relevant to unstructured proteins as Intrinsically Disordered Proteins (IDPs), for which new reaction coordinates are …

Protein FoldingChemistryOpen problemBiophysicsProteinsSequence (biology)Molecular Dynamics SimulationIntrinsically disordered proteinsArticleFolding (chemistry)Intrinsically Disordered ProteinsCrystallographyMolecular dynamicsSide chainBiophysicsHumansThermodynamicsGeneral Materials ScienceProtein foldingAmino Acid SequencePhysical and Theoretical ChemistryPeptidesPeptide sequenceThe journal of physical chemistry letters
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Aggregation processes of intrinsically disordered proteins: influence of the environment

Protein aggregation neurodegenerative diseases intrinsically disordered proteins beta amyloid peptide alpha-synucleinSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)
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Investigation of Phosphorylation-Induced Folding of an Intrinsically Disordered Protein by Coarse-Grained Molecular Dynamics

2021

Apart from being the most common mechanism of regulating protein function and transmitting signals throughout the cell, phosphorylation has an ability to induce disorder-to-order transition in an intrinsically disordered protein. In particular, it was shown that folding of the intrinsically disordered protein, eIF4E-binding protein isoform 2 (4E-BP2), can be induced by multisite phosphorylation. Here, the principles that govern the folding of phosphorylated 4E-BP2 (pT37pT46 4E-BP2(18–62)) are investigated by analyzing canonical and replica exchange molecular dynamics trajectories, generated with the coarse-grained united-residue force field, in terms of local and global motions and the time…

Protein isoformPhysicsProtein functionProtein Folding010304 chemical physicsMolecular Dynamics Simulation01 natural sciencesForce field (chemistry)ArticleComputer Science ApplicationsFolding (chemistry)Standing waveIntrinsically Disordered Proteinssymbols.namesakeMolecular dynamicsChemical physics0103 physical sciencessymbolsPhosphorylationThermodynamicsPhysical and Theoretical ChemistryPhosphorylationNonlinear Schrödinger equation
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Proteins encoded in genomic regions associated with immune-mediated disease physically interact and suggest underlying biology.

2011

Genome-wide association studies (GWAS) have defined over 150 genomic regions unequivocally containing variation predisposing to immune-mediated disease. Inferring disease biology from these observations, however, hinges on our ability to discover the molecular processes being perturbed by these risk variants. It has previously been observed that different genes harboring causal mutations for the same Mendelian disease often physically interact. We sought to evaluate the degree to which this is true of genes within strongly associated loci in complex disease. Using sets of loci defined in rheumatoid arthritis (RA) and Crohn's disease (CD) GWAS, we build protein-protein interaction (PPI) netw…

Proteins encoded genomic regions immune-mediated physically biologySettore MED/09 - Medicina Interna
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Proteomics highlights metabolic changes associated with n-hexadecane utilization in a Streptomyces coelicolor engineered strain.

2011

Proteomics n-hexadecane utilization Streptomyces coelicolor genetically engineered strain.
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Increased oxidative stress and impaired antioxidant response in Lafora disease.

2014

15 páginas, 10 figuras

ProteomicsGenetically modified mouseAntioxidantmedicine.medical_treatmentNeuroscience (miscellaneous)Proteomic analysisMice TransgenicBiologymedicine.disease_causeBiochemistryAntioxidantsLafora diseaseMiceCellular and Molecular NeuroscienceLaforinPhysiology (medical)AutophagymedicineAnimalsHumansLafora diseaseMice Knockoutchemistry.chemical_classificationReactive oxygen speciesAutophagymedicine.diseaseMalinCell biologyNeurologychemistryBiochemistryOxidative stressMutationAntioxidant enzymesReactive Oxygen SpeciesLaforinOxidative stressIntracellularFree radical biologymedicine
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Emergency Clinical Trials

2010

Emergency clinical trials involve the administration of the study drug to healthy human volunteers or to patients under the supervision of a qualified investigator, usually a physician, pursuant to a reviewed protocol. Research in this field continues to grow because this department is often considered as a desirable place to conduct clinical research due to the broad and undifferentiated spectrum of acute conditions encountered. There are some specific aspects when studying emergency medicine that have to be taken into account. One of them is the emphasis on ultrarapid diagnosis and treatment to save the critically ill emergency patient. Keywords: emergency medicine; clinical trials; diagn…

Protocol (science)Clinical trialmedicine.medical_specialtyStudy drugClinical researchCritically illbusiness.industrymedicineMedical emergencyIntensive care medicinebusinessmedicine.disease
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